We are grateful to J. Bernhagen for helpful discussions and to K. Alexandrov and R. S. Goody for help with analysis of fluorescence data. We thank A. Kazantzis, K. Tenidis, M. Waldner, H. Vasen, and M. Müsken for peptide synthesis and D. Bächle, PANATecs GmbH, R. Fischer, and H. Kalbacher for MALDI measurements. This work was supported in part by the Deutsche Forschungsgemeinschaft (DFG). Aβ=β-amyloid peptide; IAPP=islet amyloid polypeptide.
IAPP Mimic Blocks Aβ Cytotoxic Self-Assembly: Cross-Suppression of Amyloid Toxicity of Aβ and IAPP Suggests a Molecular Link between Alzheimer's Disease and Type II Diabetes†
Article first published online: 4 JAN 2007
Copyright © 2007 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Angewandte Chemie International Edition
Volume 46, Issue 8, pages 1246–1252, February 12, 2007
How to Cite
Yan, L.-M., Velkova, A., Tatarek-Nossol, M., Andreetto, E. and Kapurniotu, A. (2007), IAPP Mimic Blocks Aβ Cytotoxic Self-Assembly: Cross-Suppression of Amyloid Toxicity of Aβ and IAPP Suggests a Molecular Link between Alzheimer's Disease and Type II Diabetes. Angew. Chem. Int. Ed., 46: 1246–1252. doi: 10.1002/anie.200604056
- Issue published online: 5 FEB 2007
- Article first published online: 4 JAN 2007
- Manuscript Received: 3 OCT 2006
- Deutsche Forschungsgemeinschaft
- Alzheimer's disease;
- amyloid fibrils;
- protein design;
Le fabuleux destin d'amyloid disease: A peptide-derived inhibitor for amyloid diseases binds the Alzheimer's disease β-amyloid peptide (Aβ40) and the type II diabetes islet amyloid polypeptide (IAPP) and blocks cytotoxic self-assembly of both peptides. Evidence is also presented for a high-affinity interaction between Aβ40 and IAPP that results in cross-suppression of cytotoxic self-association of both peptides.